title: The membrane-proximal "stem" region increases the stability of the flavivirus E protein postfusion trimer and modulates its structure.
abstract: The flavivirus fusion protein E contains a "stem" region which is hypothesized to be crucial for driving fusion. This sequence element connects the ectodomain to the membrane anchor, and its structure in the trimeric postfusion conformation is still poorly defined. Using E trimers of tick-borne encephalitis virus with stem truncations of different lengths, we show that the N-terminal part of the stem increases trimer stability and also modulates the trimer structure outside the stem interaction site.
authors.affiliation: Department of Virology, Medical University of Vienna, Vienna, Austria. karin.stiasny@meduniwien.ac.at
authors.forename: Karin
authors.initials: K
authors.lastname: Stiasny
authors.forename: Stefan
authors.initials: S
authors.lastname: Kiermayr
authors.forename: Andrea
authors.initials: A
authors.lastname: Bernhart
authors.forename: Franz X
authors.initials: FX
authors.lastname: Heinz
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D004669:Encephalitis Viruses, Tick-Borne / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D005416:Flavivirus / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D054730:Protein Interaction Domains and Motifs; D055503:Protein Multimerization; D055550:Protein Stability; D020836:Protein Structure, Quaternary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D014760:Viral Fusion Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D053586:Virus Internalization
chemical_list: D011994:Recombinant Proteins; D014760:Viral Fusion Proteins